PuSH - Publication Server of Helmholtz Zentrum München: His164 regulates accessibility to the active site in fungal 17β-hydroxysteroid dehydrogenase.

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Kristan, K.* ; Adamski, J. ; Lanisnik Rizner, T.* ; Stojan, J.*

His164 regulates accessibility to the active site in fungal 17β-hydroxysteroid dehydrogenase.

Biochimie 89, 63-71 (2007)

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17ß-Hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus (17ß-HSDcl) is an NADPH-dependent member of the short-chain dehydrogenase/ reductase superfamily. To study the catalytic properties of this enzyme, we prepared several specific mutations of 17ß-HSDcl (Tyr167Phe, His164Trp/Gly, Tyr212Ala). Wild-type 17ß-HSDcl and the 17ß-HSDcl mutants were evaluated by chromatographic, kinetic and thermodynamic means. The Tyr167Phe mutation resulted in a complete loss of enzyme activity, while substitution of His164 with Trp and Gly both resulted in higher specificity number (V/K) for the steroid substrates, which are mainly a consequence of easier accessibility of steroid substrates to the active-site hollow under optimized conditions. The Tyr212Ala mutant showed increased activity in the oxidative direction, which appears to be a consequence of increased NADPH dissociation. The kinetic characterizations and thermodynamic analyses also suggest that His164 and Tyr212 in 17ß-HSDcl have a role in the opening and closing of the active site of this enzyme and in the discrimination between oxidized and reduced coenzyme.

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